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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.

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Related Experiment Video

Updated: Jul 15, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

How synaptotagmin promotes membrane fusion.

Sascha Martens1, Michael M Kozlov, Harvey T McMahon

  • 1Medical Research Council-Laboratory of Molecular Biology, Hills Road, CB2 0QH Cambridge, UK.

Science (New York, N.Y.)
|May 5, 2007
PubMed
Summary

Synaptotagmin-1, a calcium sensor, lowers the energy barrier for membrane fusion. It promotes SNARE-mediated vesicle exocytosis by inducing membrane curvature upon calcium binding.

Area of Science:

  • Molecular Biology
  • Neuroscience
  • Biophysics

Background:

  • Neurotransmitter release relies on synaptic vesicle exocytosis, a process regulated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins.
  • Fast calcium ion (Ca2+) influx triggers exocytosis, with synaptotagmin-1 identified as the critical Ca2+ sensor for rapid vesicle fusion.
  • Membrane fusion, particularly bilayer-bilayer fusion, faces a substantial activation energy barrier (approx. 40 k(B)T).

Purpose of the Study:

  • To elucidate the mechanism by which synaptotagmin-1 facilitates SNARE-mediated membrane fusion.
  • To investigate how synaptotagmin-1 overcomes the high activation energy barrier for vesicle fusion.

Main Methods:

  • Investigated the role of synaptotagmin-1's C2 domain in membrane interaction and fusion.

More Related Videos

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Related Experiment Videos

Last Updated: Jul 15, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

  • Analyzed the biophysical effects of Ca2+ binding to synaptotagmin-1 on membrane curvature and SNARE complex function.

    • Main Results:

    • Ca2+ binding to synaptotagmin-1 induces high positive curvature in target membranes via C2-domain insertion.
    • This induced membrane curvature significantly lowers the activation energy for bilayer-bilayer fusion.
    • Synaptotagmin-1 triggers docked vesicle fusion through Ca2+-dependent plasma membrane buckling and SNARE complex zippering.

    Conclusions:

    • Synaptotagmin-1 acts as a crucial regulator of membrane fusion by actively reducing the energy landscape.
    • The mechanism involves Ca2+-triggered membrane deformation, facilitating SNARE-driven fusion.
    • This Ca2+-dependent membrane buckling and SNARE zippering mechanism may represent a conserved pathway for membrane fusion events.